Product: Phospho-Fyn (Tyr530)[Tyr531] Antibody
Catalog: AF3102
Description: Rabbit polyclonal antibody to Phospho-Fyn (Tyr530)[Tyr531]
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Sheep, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 59kDa; 61kD(Calculated).
Uniprot: P06241
RRID: AB_2834539

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Product Info

WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Pig(100%), Bovine(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(91%), Xenopus(91%)
Phospho-Fyn (Tyr530) Antibody detects endogenous levels of Fyn only when phosphorylated at Tyr531, which site historically referenced as Tyr530.
Cite Format: Affinity Biosciences Cat# AF3102, RRID:AB_2834539.
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


C syn protooncogene; Fyn; FYN oncogene related to SRC FGR YES; FYN_HUMAN; OKT3 induced calcium influx regulator; P59 FYN; p59-Fyn; Protein tyrosine kinase fyn; Proto oncogene tyrosine protein kinase fyn; Proto-oncogene c-Fyn; Proto-oncogene Syn; Protooncogene Syn; SLK; Src like kinase; Src yes related novel gene; Src-like kinase; Src/yes related novel; SYN; Tyrosine kinase p59fyn T; Tyrosine kinase p59fyn(T); Tyrosine-protein kinase Fyn;



Isoform 1 is highly expressed in the brain. Isoform 2 is expressed in cells of hemopoietic lineages, especially T-lymphocytes.

FANCD2 Required for maintenance of chromosomal stability. Promotes accurate and efficient pairing of homologs during meiosis. Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing. May participate in S phase and G2 phase checkpoint activation upon DNA damage. Plays a role in preventing breakage and loss of missegregating chromatin at the end of cell division, particularly after replication stress. Required for the targeting, or stabilization, of BLM to non-centromeric abnormal structures induced by replicative stress.



Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P06241 As Substrate

Site PTM Type Enzyme
G2 Myristoylation
T12 Phosphorylation P54646 (PRKAA2)
K13 Ubiquitination
S21 Phosphorylation P17612 (PRKACA)
S25 Phosphorylation
S26 Phosphorylation
Y28 Phosphorylation P06241 (FYN) , P09619 (PDGFRB)
Y30 Phosphorylation P06241 (FYN)
Y39 Phosphorylation P06241 (FYN)
Y91 Phosphorylation
S178 Phosphorylation
T181 Phosphorylation
K182 Ubiquitination
Y185 Phosphorylation
S186 Phosphorylation
S188 Phosphorylation
K196 Ubiquitination
Y213 Phosphorylation
Y214 Phosphorylation
T217 Phosphorylation
S257 Phosphorylation
K259 Ubiquitination
K261 Ubiquitination
K275 Ubiquitination
T289 Phosphorylation
T294 Phosphorylation
K299 Ubiquitination
T300 Phosphorylation
K302 Ubiquitination
S307 Phosphorylation
K319 Ubiquitination
Y339 Phosphorylation
S349 Phosphorylation
K355 Ubiquitination
K405 Ubiquitination
Y420 Phosphorylation P06241 (FYN)
T421 Phosphorylation
K427 Ubiquitination
K431 Ubiquitination
Y440 Phosphorylation
Y483 Phosphorylation
T525 Phosphorylation
T527 Phosphorylation
Y531 Phosphorylation P41240 (CSK)

PTMs - P06241 As Enzyme

Substrate Site Source
A8K4G0 (CD300LB) Y188 Uniprot
O14522-1 (PTPRT) Y915 Uniprot
O14522-1 (PTPRT) Y1030 Uniprot
O14559 (ARHGAP33) Y406 Uniprot
O15117 (FYB1) Y559 Uniprot
O15117 (FYB1) Y571 Uniprot
O15117 (FYB1) Y595 Uniprot
O15117 (FYB1) Y625 Uniprot
O15117 (FYB1) Y651 Uniprot
O15117-2 (FYB1) Y697 Uniprot
O15117 (FYB1) Y755 Uniprot
O15117 (FYB1) Y757 Uniprot
O15117 (FYB1) Y771 Uniprot
O15117 (FYB1) Y780 Uniprot
O43294 (TGFB1I1) Y60 Uniprot
O43490 (PROM1) Y828 Uniprot
O43490 (PROM1) Y852 Uniprot
O43561 (LAT) Y200 Uniprot
O43561 (LAT) Y220 Uniprot
O60500 (NPHS1) Y1193 Uniprot
O60716 (CTNND1) Y112 Uniprot
O75674-1 (TOM1L1) Y460 Uniprot
O75886 (STAM2) Y291 Uniprot
O75886 (STAM2) Y371 Uniprot
O75886 (STAM2) Y374 Uniprot
O75955 (FLOT1) Y160 Uniprot
P00519 (ABL1) Y70 Uniprot
P00519 (ABL1) Y115 Uniprot
P00519 (ABL1) Y128 Uniprot
P00519 (ABL1) Y139 Uniprot
P00519 (ABL1) Y172 Uniprot
P00519 (ABL1) Y185 Uniprot
P00519 (ABL1) Y215 Uniprot
P00519 (ABL1) Y226 Uniprot
P00519 (ABL1) Y393 Uniprot
P05067 (APP) Y757 Uniprot
P06127 (CD5) Y453 Uniprot
P06127 (CD5) Y487 Uniprot
P06241 (FYN) Y28 Uniprot
P06241-1 (FYN) Y30 Uniprot
P06241 (FYN) Y39 Uniprot
P06241-3 (FYN) Y365 Uniprot
P06241-2 (FYN) Y417 Uniprot
P06241 (FYN) Y420 Uniprot
P07766 (CD3E) Y188 Uniprot
P07766 (CD3E) Y199 Uniprot
P10586-2 (PTPRF) Y1852 Uniprot
P10586-1 (PTPRF) Y1861 Uniprot
P10636 (MAPT) Y18 Uniprot
P10747 (CD28) Y191 Uniprot
P11137-3 (MAP2) Y50 Uniprot
P11137 (MAP2) Y67 Uniprot
P11274 (BCR) Y177 Uniprot
P11912-2 (CD79A) Y161 Uniprot
P11912 (CD79A) Y199 Uniprot
P12318-2 (FCGR2A) Y280 Uniprot
P12318 (FCGR2A) Y281 Uniprot
P12318-2 (FCGR2A) Y287 Uniprot
P12318 (FCGR2A) Y288 Uniprot
P12318-2 (FCGR2A) Y303 Uniprot
P12318 (FCGR2A) Y304 Uniprot
P14923 (JUP) Y133 Uniprot
P14923 (JUP) Y550 Uniprot
P16284 (PECAM1) Y690 Uniprot
P16284 (PECAM1) Y713 Uniprot
P16410-1 (CTLA4) Y201 Uniprot
P16410 (CTLA4) Y218 Uniprot
P16885 (PLCG2) Y743 Uniprot
P16885 (PLCG2) Y753 Uniprot
P16885 (PLCG2) Y759 Uniprot
P20916-1 (MAG) Y620 Uniprot
P20963 (CD247) Y111 Uniprot
P20963 (CD247) Y123 Uniprot
P22681 (CBL) Y700 Uniprot
P22681 (CBL) Y731 Uniprot
P22681 (CBL) Y774 Uniprot
P24666-2 (ACP1) Y132 Uniprot
P24666-1 (ACP1) Y133 Uniprot
P29353-7 (SHC1) Y318 Uniprot
P29353 (SHC1) Y349 Uniprot
P29353 (SHC1) Y350 Uniprot
P29353 (SHC1) Y427 Uniprot
P30419 (NMT1) Y180 Uniprot
P31994 (FCGR2B) Y292 Uniprot
P35222 (CTNNB1) Y142 Uniprot
P35354 (PTGS2) Y446 Uniprot
P35568 (IRS1) Y896 Uniprot
P35568 (IRS1) Y1179 Uniprot
P35612 (ADD2) Y489 Uniprot
P35637 (FUS) Y526 Uniprot
P37840-1 (SNCA) Y125 Uniprot
P40259-2 (CD79B) Y92 Uniprot
P40259-2 (CD79B) Y103 Uniprot
P40259 (CD79B) Y196 Uniprot
P40259-1 (CD79B) Y207 Uniprot
P42681 (TXK) Y420 Uniprot
P42768 (WAS) Y291 Uniprot
P43146 (DCC) Y1420 Uniprot
P49023-2 (PXN) Y118 Uniprot
P51812 (RPS6KA3) Y470 Uniprot
P51812 (RPS6KA3) Y483 Uniprot
P51812 (RPS6KA3) Y488 Uniprot
P51812 (RPS6KA3) Y529 Uniprot
P51812 (RPS6KA3) Y580 Uniprot
P51812 (RPS6KA3) Y644 Uniprot
P51812 (RPS6KA3) Y707 Uniprot
P51911-1 (CNN1) Y182 Uniprot
P51911-1 (CNN1) Y261 Uniprot
P52757 (CHN2) Y21 Uniprot
P78352 (DLG4) Y523 Uniprot
P84243 (H3F3B) S11 Uniprot
Q00535-1 (CDK5) Y15 Uniprot
Q01628 (IFITM3) Y20 Uniprot
Q03135 (CAV1) Y14 Uniprot
Q05397 (PTK2) Y576 Uniprot
Q05655 (PRKCD) Y313 Uniprot
Q05655 (PRKCD) Y334 Uniprot
Q06124 (PTPN11) Y546 Uniprot
Q07912-1 (TNK2) Y284 Uniprot
Q12879 (GRIN2A) Y943 Uniprot
Q12879 (GRIN2A) Y1105 Uniprot
Q12879 (GRIN2A) Y1118 Uniprot
Q12879 (GRIN2A) Y1187 Uniprot
Q12879 (GRIN2A) Y1246 Uniprot
Q12879 (GRIN2A) Y1267 Uniprot
Q12879 (GRIN2A) Y1325 Uniprot
Q12913 (PTPRJ) Y1311 Uniprot
Q12913 (PTPRJ) Y1320 Uniprot
Q13224 (GRIN2B) Y932 Uniprot
Q13224 (GRIN2B) Y1039 Uniprot
Q13224 (GRIN2B) Y1070 Uniprot
Q13224 (GRIN2B) Y1109 Uniprot
Q13224 (GRIN2B) Y1252 Uniprot
Q13224 (GRIN2B) Y1336 Uniprot
Q13224 (GRIN2B) Y1474 Uniprot
Q13291 (SLAMF1) Y281 Uniprot
Q13291-1 (SLAMF1) Y307 Uniprot
Q13291 (SLAMF1) Y327 Uniprot
Q13322-3 (GRB10) Y9 Uniprot
Q13322 (GRB10) Y67 Uniprot
Q14194 (CRMP1) Y504 Uniprot
Q14254 (FLOT2) Y163 Uniprot
Q14524 (SCN5A) Y1494 Uniprot
Q14524 (SCN5A) Y1495 Uniprot
Q14643 (ITPR1) Y353 Uniprot
Q15417-1 (CNN3) Y261 Uniprot
Q15762 (CD226) Y322 Uniprot
Q15831 (STK11) Y261 Uniprot
Q15831 (STK11) Y362 Uniprot
Q16236 (NFE2L2) Y576 Uniprot
Q16539 (MAPK14) Y323 Uniprot
Q16555 (DPYSL2) Y32 Uniprot
Q6ZMQ8 (AATK) Y73 Uniprot
Q6ZMQ8 (AATK) Y93 Uniprot
Q86WV1 (SKAP1) Y219 Uniprot
Q86WV1 (SKAP1) Y232 Uniprot
Q86WV1 (SKAP1) Y295 Uniprot
Q86WV1 (SKAP1) Y298 Uniprot
Q8TDQ1 (CD300LF) Y236 Uniprot
Q8TDQ1 (CD300LF) Y263 Uniprot
Q96J02 (ITCH) Y420 Uniprot
Q96J84 (KIRREL1) Y572 Uniprot
Q96J84 (KIRREL1) Y605 Uniprot
Q96J84 (KIRREL1) Y622 Uniprot
Q96LC7 (SIGLEC10) Y667 Uniprot
Q99490-2 (AGAP2) Y682 Uniprot
Q99490-2 (AGAP2) Y774 Uniprot
Q99490 (AGAP2) Y1038 Uniprot
Q99490 (AGAP2) Y1130 Uniprot
Q9H204 (MED28) Y64 Uniprot
Q9NQC3 (RTN4) Y694 Uniprot
Q9NRY4 (ARHGAP35) Y1087 Uniprot
Q9NRY4 (ARHGAP35) Y1105 Uniprot
Q9NZA1 (CLIC5) Y33 Uniprot

Research Backgrounds


Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1. In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (By similarity).


Autophosphorylated at Tyr-420 (By similarity). Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state. PTPRC/CD45 dephosphorylates Tyr-531 leading to activation. Ultraviolet B (UVB) strongly increase phosphorylation at Thr-12 and kinase activity, and promotes translocation from the cytoplasm to the nucleus. Dephosphorylation at Tyr-420 by PTPN2 negatively regulates T-cell receptor signaling. Phosphorylated at tyrosine residues, which can be enhanced by NTN1 (By similarity).

Palmitoylation at Cys-3 and Cys-6 regulates subcellular location.

Subcellular Location:

Cytoplasm. Nucleus. Cell membrane.
Note: Present and active in lipid rafts. Palmitoylation is crucial for proper trafficking.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Isoform 1 is highly expressed in the brain. Isoform 2 is expressed in cells of hemopoietic lineages, especially T-lymphocytes.

Subunit Structure:

Interacts (via its SH3 domain) with PIK3R1 and PRMT8. Interacts with FYB1, PAG1, and SH2D1A. Interacts with CD79A (tyrosine-phosphorylated form); the interaction increases FYN activity. Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated) (By similarity). Interacts with TOM1L1 (phosphorylated form). Interacts with KDR (tyrosine phosphorylated). Interacts (via SH3 domain) with KLHL2 (via N-terminus) (By similarity). Interacts with SH2D1A and SLAMF1. Interacts with ITCH; the interaction phosphorylates ITCH and negatively regulates its activity. Interacts with FASLG. Interacts with RUNX3. Interacts with KIT. Interacts with EPHA8; possible downstream effector of EPHA8 in regulation of cell adhesion. Interacts with PTK2/FAK1; this interaction leads to PTK2/FAK1 phosphorylation and activation. Interacts with CAV1; this interaction couples integrins to the Ras-ERK pathway. Interacts with UNC119. Interacts (via SH2 domain) with PTPRH (phosphorylated form) (By similarity). Interacts with PTPRO (phosphorylated form) (By similarity). Interacts with PTPRB (phosphorylated form) (By similarity). Interacts with FYB2. Interacts with DSCAM (By similarity). Interacts with SKAP1 and FYB1; this interaction promotes the phosphorylation of CLNK (By similarity).

(Microbial infection) Interacts (via its SH3 domain) with hepatitis E virus/HEV protein ORF3.


Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Research Fields

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Adherens junction.   (View pathway)

· Environmental Information Processing > Signal transduction > Sphingolipid signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Phospholipase D signaling pathway.   (View pathway)

· Human Diseases > Neurodegenerative diseases > Prion diseases.

· Human Diseases > Infectious diseases: Bacterial > Pathogenic Escherichia coli infection.

· Human Diseases > Infectious diseases: Viral > Measles.

· Human Diseases > Cardiovascular diseases > Viral myocarditis.

· Organismal Systems > Development > Axon guidance.   (View pathway)

· Organismal Systems > Development > Osteoclast differentiation.   (View pathway)

· Organismal Systems > Immune system > Platelet activation.   (View pathway)

· Organismal Systems > Immune system > Natural killer cell mediated cytotoxicity.   (View pathway)

· Organismal Systems > Immune system > T cell receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > Fc epsilon RI signaling pathway.   (View pathway)

· Organismal Systems > Nervous system > Cholinergic synapse.


1). Oxyberberine, an absorbed metabolite of berberine, possess superior hypoglycemic effect via regulating the PI3K/Akt and Nrf2 signaling pathways. BIOMEDICINE & PHARMACOTHERAPY, 2021 (PubMed: 33524788) [IF=7.5]

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